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Yohanis Mandik
Universitas Cenderawasih
Chemistry

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KARAKTERISASI PRODUK GEN PENGKODE CHAPERONE BACILLUS SP. RP1 Kumaunang, Maureen; Mandik, Yohanis
CHEMISTRY PROGRESS Vol 3, No 1 (2010)
Publisher : Sam Ratulangi University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35799/cp.3.1.2010.75

Abstract

Molecular chaperone is the group of protein that assist in the correct folding or assembly of other proteins invivo. The objective of this research was to characterize the product of gene encoding chaperone from Bacillussp. RP1 by using in-silico analysis. Analysis of 1053 bp from DNA fragment isolated by PCR showed that it has97% similarity with putative chaperone of Geobacillus kaustophilus (BA000043.1) and 86% similarity with DnaKoperon of B. stearothermophilus (X90709.1). Structure prediction of DnaJ Bacillus sp. RP1 showed that it hassimilar J-domain with that of DnaJ Escherichia coli but cys-rich domain is different.
ANALISIS IN-SILICO PROTEIN DnaJ Bacilus stearothermophilus Kumaunang, Maureen; Kamu, Vanda S.; Mandik, Yohanis I.
CHEMISTRY PROGRESS Vol 2, No 1 (2009)
Publisher : Sam Ratulangi University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35799/cp.2.1.2009.63

Abstract

DnaJ is a chaperone which has function in facilitating folding, translocation, and degradation of protein.The aim of this research was to undertake in silico study of DnaJ protein from Bacillus stearothermophilus.Structure analysis of DnaJ B. stearothermophilus showed that it has J-domain which has two conservedmotifs, i.e. HPD and QKRA motifs. It also has cys-rich domain which has one conserved motif, i.e.CXXCXGXG. Structure prediction of DnaJ B. stearothermophilus showed that it has similar structure of Jdomainand cys-rich domain with that of DnaJ Escherichia coli.
Co-Authors Maureen Kumaunang Vanda S. Kamu